ID SRGP2_HUMAN Reviewed; 1071 AA. AC O75044; A2RUF3; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2017, sequence version 3. DT 16-JAN-2019, entry version 167. DE RecName: Full=SLIT-ROBO Rho GTPase-activating protein 2; DE Short=srGAP2; DE AltName: Full=Formin-binding protein 2; DE AltName: Full=Rho GTPase-activating protein 34; GN Name=SRGAP2; Synonyms=ARHGAP34, FNBP2, KIAA0456, SRGAP2A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=9455484; DOI=10.1093/dnares/4.5.345; RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., RA Nomura N., Ohara O.; RT "Characterization of cDNA clones in size-fractionated cDNA libraries RT from human brain."; RL DNA Res. 4:345-349(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP INTERACTION WITH ROBO1. RX PubMed=11672528; DOI=10.1016/S0092-8674(01)00530-X; RA Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H., RA Wen L., Brady-Kalnay S.M., Mei L., Wu J.Y., Xiong W.C., Rao Y.; RT "Signal transduction in neuronal migration: roles of GTPase activating RT proteins and the small GTPase Cdc42 in the Slit-Robo pathway."; RL Cell 107:209-221(2001). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP INTERACTION WITH FASLG. RX PubMed=19807924; DOI=10.1186/1471-2172-10-53; RA Voss M., Lettau M., Janssen O.; RT "Identification of SH3 domain interaction partners of human FasL RT (CD178) by phage display screening."; RL BMC Immunol. 10:53-53(2009). RN [9] RP FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION, INTERACTION WITH RP PRMT5, METHYLATION AT ARG-927 BY PRMT5, AND MUTAGENESIS OF ARG-927. RX PubMed=20810653; DOI=10.1074/jbc.M110.153429; RA Guo S., Bao S.; RT "srGAP2 arginine methylation regulates cell migration and cell RT spreading through promoting dimerization."; RL J. Biol. Chem. 285:35133-35141(2010). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP CHROMOSOMAL REARRANGEMENT. RX PubMed=22106086; DOI=10.1002/ajmg.a.34363; RA Saitsu H., Osaka H., Sugiyama S., Kurosawa K., Mizuguchi T., RA Nishiyama K., Nishimura A., Tsurusaki Y., Doi H., Miyake N., RA Harada N., Kato M., Matsumoto N.; RT "Early infantile epileptic encephalopathy associated with the RT disrupted gene encoding Slit-Robo Rho GTPase activating protein 2 RT (SRGAP2)."; RL Am. J. Med. Genet. A 158A:199-205(2012). RN [14] RP FUNCTION IN ACTIN FILAMENT SEVERING, RAC1 GAP ACTIVITY, INTERACTION RP WITH FMNL1; FMNL3 AND ROBO2, AND SUBCELLULAR LOCATION. RX PubMed=21148482; DOI=10.1074/jbc.M110.190397; RA Mason F.M., Heimsath E.G., Higgs H.N., Soderling S.H.; RT "Bi-modal regulation of a formin by srGAP2."; RL J. Biol. Chem. 286:6577-6586(2011). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SRGAP2C. RX PubMed=22559944; DOI=10.1016/j.cell.2012.03.034; RA Charrier C., Joshi K., Coutinho-Budd J., Kim J.E., Lambert N., RA de Marchena J., Jin W.L., Vanderhaeghen P., Ghosh A., Sassa T., RA Polleux F.; RT "Inhibition of SRGAP2 function by its human-specific paralogs induces RT neoteny during spine maturation."; RL Cell 149:923-935(2012). RN [16] RP HETEROOLIGOMERIZATION, AND DOMAIN F-BAR. RX PubMed=22467852; DOI=10.1242/jcs.098962; RA Coutinho-Budd J., Ghukasyan V., Zylka M.J., Polleux F.; RT "The F-BAR domains from srGAP1, srGAP2, and srGAP3 differentially RT regulate membrane deformation."; RL J. Cell Sci. 125:3390-3401(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-795; SER-916; SER-994; RP SER-1013 AND SER-1027, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP STRUCTURE BY NMR OF 729-787. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH3 domain of human SLIT-ROBO Rho GTPase- RT activating protein 2."; RL Submitted (OCT-2006) to the PDB data bank. CC -!- FUNCTION: RAC1 GTPase activating protein (GAP) that binds and CC deforms membranes, and regulates actin dynamics to regulate cell CC migration and differentiation. Plays an important role in CC different aspects of neuronal morphogenesis and migration mainly CC during development of the cerebral cortex. This includes the CC biogenesis of neurites, where it is required for both axons and CC dendrites outgrowth, and the maturation of the dendritic spines. CC Also stimulates the branching of the leading process and CC negatively regulates neuron radial migration in the cerebral CC cortex. Its interaction and inhibition by SRGAP2C reduces the rate CC of spine maturation, alters dendritic spine morphology and density CC and indirectly increases neuronal migration. It may have CC implications for cognition, learning and memory. In non-neuronal CC cells, it may also play a role in cell migration by regulating the CC formation of lamellipodia and filopodia. CC {ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21148482, CC ECO:0000269|PubMed:22559944}. CC -!- SUBUNIT: Homodimer (Probable). Forms a heterooligomer with SRGAP1 CC and SRGAP3 through its F-BAR domain. Interacts (via SH3 domain) CC with GPHN (By similarity). Interacts with SRGAP2C; formation of CC the heterodimer alters SRGAP2 function. Interacts (via SH3 domain) CC with FMNL1 (activated by RAC1); regulates the actin filament CC severing activity of FMNL1 and actin dynamics. Interacts (via SH3 CC domain) with FMNL3. Interacts with RAC1; specifically stimulates CC RAC1 GTPase activity. Probably interacts with ROBO1 and ROBO2. CC Interacts with FASLG. Interacts with PRMT5. {ECO:0000250, CC ECO:0000269|PubMed:11672528, ECO:0000269|PubMed:19807924, CC ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21148482, CC ECO:0000269|PubMed:22559944, ECO:0000305}. CC -!- INTERACTION: CC Self; NbExp=5; IntAct=EBI-1051034, EBI-1051034; CC P48023:FASLG; NbExp=2; IntAct=EBI-1051034, EBI-495538; CC O95466:FMNL1; NbExp=3; IntAct=EBI-1051034, EBI-720020; CC P42858:HTT; NbExp=3; IntAct=EBI-1051034, EBI-466029; CC O14744:PRMT5; NbExp=4; IntAct=EBI-1051034, EBI-351098; CC Q9Y6N7:ROBO1; NbExp=3; IntAct=EBI-1051034, EBI-399762; CC -!- SUBCELLULAR LOCATION: Cell membrane. Cell projection, dendritic CC spine. Cell junction, synapse, postsynaptic cell membrane, CC postsynaptic density {ECO:0000250}. Cell junction, synapse, CC postsynaptic cell membrane {ECO:0000250}. Cell projection, CC lamellipodium. Cytoplasmic vesicle, phagosome {ECO:0000250}. CC Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Recruited to CC actin-rich phagosomes during phagocytosis. Translocates from CC nucleus to cytoplasm during development. {ECO:0000250}. CC -!- DOMAIN: The F-BAR domain mediates oligomerization, binds CC membranes, and induces plasma membrane protrusions. CC {ECO:0000269|PubMed:22467852}. CC -!- PTM: Methylation at Arg-927 is required for the stimulation of CC cell migration, dimerization and localization at the plasma CC membrane protrusions. {ECO:0000269|PubMed:20810653}. CC -!- DISEASE: Note=A chromosomal aberration disrupting SRGAP2 has been CC found in a patient with early infantile epileptic encephalopathy. CC Balanced translocation t(1;9)(q32;q13) (PubMed:22106086). CC {ECO:0000269|PubMed:22106086}. CC -!- MISCELLANEOUS: There are 3 duplications of SRGAP2 in the human CC genome as a result of segmental gene duplications. SRGAP2C is the CC only one to be fixed at a diploid state in the human genome. CC Moreover, SRGAP2C is functional, interacts with and inhibits CC SRGAP2 and is human-specific. The appearance of SRGAP2C in the CC human genome is estimated to 2,4 million years ago, which CC corresponds to the beginning of neocortex expansion in human CC evolution and it may have played an important role in this process CC through its interaction with SRGAP2 function. CC -!- SEQUENCE CAUTION: CC Sequence=BAA32301.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Branching out - Issue CC 143 of October 2012; CC URL="https://web.expasy.org/spotlight/back_issues/143"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC244023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC244034; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC244035; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC244158; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB007925; BAA32301.1; ALT_INIT; mRNA. DR EMBL; BC132872; AAI32873.1; -; mRNA. DR EMBL; BC132874; AAI32875.1; -; mRNA. DR CCDS; CCDS73017.1; -. DR PIR; C59437; C59437. DR RefSeq; NP_001164108.1; NM_001170637.3. DR RefSeq; NP_056141.2; NM_015326.4. DR RefSeq; XP_005277567.1; XM_005277510.2. DR UniGene; Hs.497575; -. DR UniGene; Hs.729527; -. DR UniGene; Hs.744555; -. DR PDB; 2DL8; NMR; -; A=729-787. DR PDB; 4RTT; X-ray; 1.87 A; A/B=729-815. DR PDB; 4RUG; X-ray; 1.73 A; A/B=729-815. DR PDB; 5I6J; X-ray; 2.70 A; A=1-484. DR PDB; 5I6R; X-ray; 2.15 A; A=1-484. DR PDB; 5I7D; X-ray; 3.95 A; A/B=1-484. DR PDBsum; 2DL8; -. DR PDBsum; 4RTT; -. DR PDBsum; 4RUG; -. DR PDBsum; 5I6J; -. DR PDBsum; 5I6R; -. DR PDBsum; 5I7D; -. DR ProteinModelPortal; O75044; -. DR SMR; O75044; -. DR BioGrid; 116956; 96. DR DIP; DIP-37618N; -. DR IntAct; O75044; 24. DR MINT; O75044; -. DR STRING; 9606.ENSP00000295713; -. DR iPTMnet; O75044; -. DR PhosphoSitePlus; O75044; -. DR BioMuta; SRGAP2; -. DR EPD; O75044; -. DR jPOST; O75044; -. DR PaxDb; O75044; -. DR PeptideAtlas; O75044; -. DR PRIDE; O75044; -. DR ProteomicsDB; 49722; -. DR DNASU; 23380; -. DR Ensembl; ENST00000573034; ENSP00000459615; ENSG00000266028. DR GeneID; 23380; -. DR KEGG; hsa:23380; -. DR UCSC; uc031vli.2; human. DR CTD; 23380; -. DR DisGeNET; 23380; -. DR EuPathDB; HostDB:ENSG00000266028.7; -. DR GeneCards; SRGAP2; -. DR H-InvDB; HIX0001527; -. DR H-InvDB; HIX0029679; -. DR H-InvDB; HIX0116247; -. DR HGNC; HGNC:19751; SRGAP2. DR HPA; HPA028191; -. DR HPA; HPA028196; -. DR MIM; 606524; gene. DR neXtProt; NX_O75044; -. DR OpenTargets; ENSG00000266028; -. DR PharmGKB; PA164742513; -. DR eggNOG; KOG3565; Eukaryota. DR eggNOG; ENOG410XS44; LUCA. DR GeneTree; ENSGT00940000153559; -. DR HOGENOM; HOG000039980; -. DR HOVERGEN; HBG051637; -. DR InParanoid; O75044; -. DR KO; K07526; -. DR OMA; GSTEDYC; -. DR OrthoDB; 1245523at2759; -. DR PhylomeDB; O75044; -. DR Reactome; R-HSA-194840; Rho GTPase cycle. DR Reactome; R-HSA-428543; Inactivation of CDC42 and RAC1. DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR ChiTaRS; SRGAP2; human. DR EvolutionaryTrace; O75044; -. DR GeneWiki; SRGAP2; -. DR GenomeRNAi; 23380; -. DR PRO; PR:O75044; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000266028; Expressed in 200 organ(s), highest expression level in right hemisphere of cerebellum. DR CleanEx; HS_SRGAP2; -. DR ExpressionAtlas; O75044; baseline and differential. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0044327; C:dendritic spine head; IDA:UniProtKB. DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB. DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0048365; F:Rac GTPase binding; IDA:UniProtKB. DR GO; GO:0051014; P:actin filament severing; IDA:UniProtKB. DR GO; GO:0060996; P:dendritic spine development; IDA:UniProtKB. DR GO; GO:0021816; P:extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration; ISS:UniProtKB. DR GO; GO:0046847; P:filopodium assembly; IDA:UniProtKB. DR GO; GO:0003363; P:lamellipodium assembly involved in ameboidal cell migration; IMP:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; IBA:GO_Central. DR GO; GO:2001223; P:negative regulation of neuron migration; IDA:UniProtKB. DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB. DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB. DR CDD; cd11955; SH3_srGAP1-3; 1. DR Gene3D; 1.10.555.10; -; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR031160; F_BAR. DR InterPro; IPR001060; FCH_dom. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR035648; srGAP1/2/3_SH3. DR InterPro; IPR030252; srGAP2. DR PANTHER; PTHR14166:SF6; PTHR14166:SF6; 1. DR Pfam; PF00611; FCH; 1. DR Pfam; PF00620; RhoGAP; 1. DR Pfam; PF00018; SH3_1; 1. DR SMART; SM00055; FCH; 1. DR SMART; SM00324; RhoGAP; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF103657; SSF103657; 1. DR SUPFAM; SSF48350; SSF48350; 1. DR SUPFAM; SSF50044; SSF50044; 1. DR PROSITE; PS51741; F_BAR; 1. DR PROSITE; PS50238; RHOGAP; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell junction; Cell membrane; Cell projection; KW Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm; KW Cytoplasmic vesicle; GTPase activation; Membrane; Methylation; KW Neurogenesis; Nucleus; Phosphoprotein; Polymorphism; KW Postsynaptic cell membrane; Reference proteome; SH3 domain; Synapse. FT CHAIN 1 1071 SLIT-ROBO Rho GTPase-activating protein FT 2. FT /FTId=PRO_0000056767. FT DOMAIN 22 325 F-BAR. {ECO:0000255|PROSITE- FT ProRule:PRU01077}. FT DOMAIN 489 679 Rho-GAP. {ECO:0000255|PROSITE- FT ProRule:PRU00172}. FT DOMAIN 728 787 SH3. {ECO:0000255|PROSITE- FT ProRule:PRU00192}. FT COILED 362 401 {ECO:0000255}. FT COILED 940 967 {ECO:0000255}. FT COMPBIAS 843 909 Ser-rich. FT MOD_RES 206 206 Phosphoserine. FT {ECO:0000250|UniProtKB:D4A208}. FT MOD_RES 427 427 Phosphoserine. FT {ECO:0000250|UniProtKB:D4A208}. FT MOD_RES 500 500 Phosphoserine. FT {ECO:0000250|UniProtKB:Q91Z67}. FT MOD_RES 691 691 Phosphoserine. FT {ECO:0000250|UniProtKB:D4A208}. FT MOD_RES 695 695 Phosphoserine. FT {ECO:0000250|UniProtKB:Q91Z67}. FT MOD_RES 724 724 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 795 795 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 916 916 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 927 927 Omega-N-methylated arginine; by PRMT5. FT {ECO:0000269|PubMed:20810653}. FT MOD_RES 930 930 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 990 990 Phosphoserine. FT {ECO:0000250|UniProtKB:Q91Z67}. FT MOD_RES 994 994 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1013 1013 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1027 1027 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT VARIANT 874 874 R -> G (in dbSNP:rs17018890). FT /FTId=VAR_055834. FT MUTAGEN 927 927 R->A: Loss of the ability to stimulate FT cell migration, to localize at the plasma FT membrane protrusions and to dimerize. FT {ECO:0000269|PubMed:20810653}. FT CONFLICT 709 709 S -> P (in Ref. 2; BAA32301). FT HELIX 10 76 {ECO:0000244|PDB:5I6R}. FT HELIX 94 122 {ECO:0000244|PDB:5I6R}. FT HELIX 124 186 {ECO:0000244|PDB:5I6R}. FT HELIX 188 191 {ECO:0000244|PDB:5I6R}. FT HELIX 223 269 {ECO:0000244|PDB:5I6R}. FT HELIX 271 278 {ECO:0000244|PDB:5I6R}. FT TURN 279 281 {ECO:0000244|PDB:5I6R}. FT HELIX 284 318 {ECO:0000244|PDB:5I6R}. FT HELIX 322 332 {ECO:0000244|PDB:5I6R}. FT HELIX 334 337 {ECO:0000244|PDB:5I6R}. FT STRAND 348 350 {ECO:0000244|PDB:5I6J}. FT HELIX 362 402 {ECO:0000244|PDB:5I6R}. FT HELIX 410 413 {ECO:0000244|PDB:5I6R}. FT HELIX 436 478 {ECO:0000244|PDB:5I6R}. FT STRAND 731 737 {ECO:0000244|PDB:4RUG}. FT STRAND 742 746 {ECO:0000244|PDB:2DL8}. FT STRAND 754 762 {ECO:0000244|PDB:4RUG}. FT STRAND 765 770 {ECO:0000244|PDB:4RUG}. FT STRAND 773 778 {ECO:0000244|PDB:4RUG}. FT HELIX 779 781 {ECO:0000244|PDB:4RUG}. FT STRAND 782 784 {ECO:0000244|PDB:4RUG}. FT HELIX 791 795 {ECO:0000244|PDB:4RUG}. FT HELIX 800 804 {ECO:0000244|PDB:4RUG}. SQ SEQUENCE 1071 AA; 120871 MW; 5693E6AF33A03E97 CRC64; MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ DFFRKKAEIE MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN LLLNQVKRES RDHTTLSDIY LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ DDLMKVLNEL YSVMKTYHMY NADSISAQSK LKEAEKQEEK QIGKSVKQED RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT ENKLKAIKAR NEYLLALEAT NASVFKYYIH DLSDLIDQCC DLGYHASLNR ALRTFLSAEL NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG DMASQLCAQQ PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD IVTVEDFDVS DCFQYSNSME SVKSTVSETF MSKPSIAKRR ANQQETEQFY FTKMKEYLEG RNLITKLQAK HDLLQKTLGE SQRTDCSLAR RSSTVRKQDS SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN AFERGEDPLA GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLMACVT MDNLQERALH IRKVLLVLPK TTLIIMRYLF AFLNHLSQFS EENMMDPYNL AICFGPSLMS VPEGHDQVSC QAHVNELIKT IIIQHENIFP SPRELEGPVY SRGGSMEDYC DSPHGETTSV EDSTQDVTAE HHTSDDECEP IEAIAKFDYV GRTARELSFK KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ YIVVQDTEDG VVERSSPKSE IEVISEPPEE KVTARAGASC PSGGHVADIY LANINKQRKR PESGSIRKTF RSDSHGLSSS LTDSSSPGVG ASCRPSSQPI MSQSLPKEGP DKCSISGHGS LNSISRHSSL KNRLDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM NSALNELREL ERQSSVKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL LKDPEPAFQR SASTAGDIAC AFRPVKSVKM AAPVKPPATR PKPTVFPKTN ATSPGVNSST SPQSTDKSCT V //